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P00636

- F16P1_PIG

UniProt

P00636 - F16P1_PIG

Protein

Fructose-1,6-bisphosphatase 1

Gene

FBP1

Organism
Sus scrofa (Pig)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 134 (01 Oct 2014)
      Sequence version 4 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Catalyzes the hydrolysis of fructose 1,6-bisphosphate to fructose 6-phosphate in the presence of divalent cations, acting as a rate-limiting enzyme in gluconeogenesis. Plays a role in regulating glucose sensing and insulin secretion of pancreatic beta-cells. Appears to modulate glycerol gluconeogenesis in liver. Important regulator of appetite and adiposity; increased expression of the protein in liver after nutrient excess increases circulating satiety hormones and reduces appetite-stimulating neuropeptides and thus seems to provide a feedback mechanism to limit weight gain By similarity.By similarity

    Catalytic activityi

    D-fructose 1,6-bisphosphate + H2O = D-fructose 6-phosphate + phosphate.

    Cofactori

    Binds 3 magnesium ions per subunit.4 Publications

    Enzyme regulationi

    Subject to complex allosteric regulation. The enzyme can assume an active R-state, or an inactive T-state. Intermediate conformations may exist. AMP acts as allosteric inhibitor. AMP binding affects the turnover of bound substrate and not the affinity for substrate. Fructose 2,6-bisphosphate acts as competitive inhibitor. Fructose 2,6-bisphosphate and AMP have synergistic effects.6 Publications

    Kineticsi

    1. KM=1.2 µM for fructose-1,6-diphosphate1 Publication

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi69 – 691Magnesium 11 Publication
    Metal bindingi98 – 981Magnesium 11 Publication
    Metal bindingi98 – 981Magnesium 21 Publication
    Metal bindingi119 – 1191Magnesium 21 Publication
    Metal bindingi119 – 1191Magnesium 31 Publication
    Metal bindingi121 – 1211Magnesium 2; via carbonyl oxygen1 Publication
    Metal bindingi122 – 1221Magnesium 31 Publication
    Binding sitei141 – 1411AMP1 Publication
    Binding sitei265 – 2651Substrate
    Metal bindingi281 – 2811Magnesium 31 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi18 – 225AMP1 Publication
    Nucleotide bindingi28 – 325AMP1 Publication
    Nucleotide bindingi113 – 1142AMP1 Publication

    GO - Molecular functioni

    1. AMP binding Source: UniProtKB
    2. fructose 1,6-bisphosphate 1-phosphatase activity Source: UniProtKB
    3. metal ion binding Source: UniProtKB
    4. monosaccharide binding Source: UniProtKB

    GO - Biological processi

    1. cellular response to drug Source: UniProtKB
    2. cellular response to magnesium ion Source: UniProtKB
    3. dephosphorylation Source: UniProtKB
    4. fructose 6-phosphate metabolic process Source: UniProtKB
    5. gluconeogenesis Source: UniProtKB
    6. negative regulation of cell growth Source: UniProtKB
    7. negative regulation of glycolytic process Source: UniProtKB
    8. negative regulation of Ras protein signal transduction Source: UniProtKB
    9. protein homotetramerization Source: UniProtKB
    10. regulation of gluconeogenesis Source: UniProtKB

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Carbohydrate metabolism, Gluconeogenesis

    Keywords - Ligandi

    Magnesium, Metal-binding

    Enzyme and pathway databases

    BRENDAi3.1.3.11. 6170.
    SABIO-RKP00636.
    UniPathwayiUPA00138.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Fructose-1,6-bisphosphatase 1 (EC:3.1.3.11)
    Short name:
    FBPase 1
    Alternative name(s):
    D-fructose-1,6-bisphosphate 1-phosphohydrolase 1
    Liver FBPase
    Gene namesi
    Name:FBP1
    Synonyms:FBP
    OrganismiSus scrofa (Pig)
    Taxonomic identifieri9823 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
    ProteomesiUP000008227: Unplaced

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. cytosol Source: UniProtKB

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi55 – 551A → L: Destabilizes the inactive T-state and promotes transition to the R-state.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 338337Fructose-1,6-bisphosphatase 1PRO_0000200500Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylthreonine2 Publications
    Modified residuei151 – 1511N6-succinyllysineBy similarity
    Modified residuei208 – 2081Phosphoserine; by PKA1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    PaxDbiP00636.
    PRIDEiP00636.

    Interactioni

    Subunit structurei

    Homotetramer.9 Publications

    Structurei

    Secondary structure

    1
    338
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi14 – 2411
    Helixi30 – 5021
    Turni51 – 566
    Beta strandi59 – 646
    Beta strandi66 – 683
    Beta strandi70 – 723
    Helixi73 – 8816
    Beta strandi92 – 976
    Beta strandi101 – 1055
    Helixi108 – 1103
    Beta strandi111 – 12212
    Helixi124 – 1263
    Turni127 – 1304
    Beta strandi133 – 1419
    Beta strandi144 – 1463
    Beta strandi147 – 1493
    Helixi150 – 1534
    Helixi157 – 1593
    Beta strandi161 – 17818
    Beta strandi181 – 1888
    Turni189 – 1924
    Beta strandi193 – 1986
    Beta strandi208 – 2114
    Helixi214 – 2196
    Helixi222 – 23211
    Beta strandi235 – 2373
    Beta strandi242 – 2454
    Helixi249 – 25911
    Beta strandi262 – 2654
    Beta strandi268 – 2703
    Turni271 – 2733
    Beta strandi275 – 2773
    Turni278 – 2814
    Helixi282 – 29110
    Beta strandi295 – 2973
    Beta strandi299 – 3024
    Helixi303 – 3053
    Beta strandi309 – 3124
    Beta strandi317 – 3204
    Helixi322 – 33413

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1CNQX-ray2.27A2-338[»]
    1EYIX-ray2.32A2-338[»]
    1EYJX-ray2.28A/B2-338[»]
    1EYKX-ray2.23A/B2-338[»]
    1FBCX-ray2.60A/B2-336[»]
    1FBDX-ray2.90A/B2-336[»]
    1FBEX-ray3.00A/B2-336[»]
    1FBFX-ray2.70A/B2-336[»]
    1FBGX-ray3.00A/B2-336[»]
    1FBHX-ray2.50A/B2-336[»]
    1FBPX-ray2.50A/B2-336[»]
    1FJ6X-ray2.50A2-338[»]
    1FJ9X-ray2.50A/B2-338[»]
    1FPBX-ray2.60A/B2-336[»]
    1FPDX-ray2.10A/B2-336[»]
    1FPEX-ray2.20A/B2-336[»]
    1FPFX-ray2.10A/B2-336[»]
    1FPGX-ray2.30A/B2-336[»]
    1FPIX-ray2.30A/B2-336[»]
    1FPJX-ray2.20A/B2-336[»]
    1FPKX-ray3.00A/B2-336[»]
    1FPLX-ray2.30A/B2-336[»]
    1FRPX-ray2.00A/B2-336[»]
    1FSAX-ray2.30A/B2-338[»]
    1KZ8X-ray2.00A/F2-338[»]
    1LEVX-ray2.15A/F2-338[»]
    1NUWX-ray1.30A2-338[»]
    1NUXX-ray1.60A2-338[»]
    1NUYX-ray1.30A2-338[»]
    1NUZX-ray1.90A2-338[»]
    1NV0X-ray1.80A2-338[»]
    1NV1X-ray1.90A2-338[»]
    1NV2X-ray2.10A2-338[»]
    1NV3X-ray2.00A2-338[»]
    1NV4X-ray1.90A2-338[»]
    1NV5X-ray1.90A2-338[»]
    1NV6X-ray2.15A2-338[»]
    1NV7X-ray2.15A/B2-338[»]
    1Q9DX-ray2.35A/B2-338[»]
    1RDXX-ray2.75A/B2-338[»]
    1RDYX-ray2.20A/B2-338[»]
    1RDZX-ray2.05A/B2-338[»]
    1YXIX-ray2.00A2-338[»]
    1YYZX-ray1.85A2-338[»]
    1YZ0X-ray2.07A/B2-338[»]
    2F3BX-ray1.80A1-338[»]
    2F3DX-ray1.83A1-338[»]
    2FBPX-ray2.80A/B2-336[»]
    2QVUX-ray1.50A/B2-338[»]
    2QVVX-ray2.03A/B2-338[»]
    3FBPX-ray2.80A/B2-336[»]
    4FBPX-ray2.50A/B/C/D2-336[»]
    4GBVX-ray2.90A2-336[»]
    4GBWX-ray2.00A2-336[»]
    4GWSX-ray2.75A/B2-338[»]
    4GWUX-ray3.00A2-338[»]
    4GWWX-ray3.20A2-338[»]
    4GWXX-ray2.35A2-338[»]
    4GWYX-ray3.00A2-338[»]
    4GWZX-ray2.60A/B2-338[»]
    4GX3X-ray2.25A/B2-338[»]
    4GX4X-ray2.50A/B2-338[»]
    4GX6X-ray2.50A/B2-338[»]
    4H45X-ray3.10A2-338[»]
    4H46X-ray2.50A2-338[»]
    4KXPX-ray2.70A/B1-338[»]
    5FBPX-ray2.10A/B2-336[»]
    ProteinModelPortaliP00636.
    SMRiP00636. Positions 7-338.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP00636.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni122 – 1254Substrate binding
    Regioni213 – 2164Substrate binding
    Regioni244 – 2496Substrate binding
    Regioni275 – 2773Substrate binding

    Sequence similaritiesi

    Belongs to the FBPase class 1 family.Curated

    Phylogenomic databases

    eggNOGiCOG0158.
    HOGENOMiHOG000191265.
    HOVERGENiHBG005627.
    KOiK03841.

    Family and domain databases

    HAMAPiMF_01855. FBPase_class1.
    InterProiIPR000146. FBPase_class-1/SBPase.
    IPR028343. FBPtase.
    IPR020548. Fructose_bisphosphatase_AS.
    [Graphical view]
    PANTHERiPTHR11556. PTHR11556. 1 hit.
    PfamiPF00316. FBPase. 1 hit.
    [Graphical view]
    PIRSFiPIRSF500210. FBPtase. 1 hit.
    PIRSF000904. FBPtase_SBPase. 1 hit.
    PRINTSiPR00115. F16BPHPHTASE.
    PROSITEiPS00124. FBPASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P00636-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTDQAAFDTN IVTLTRFVME EGRKARGTGE MTQLLNSLCT AVKAISTAVR    50
    KAGIAHLYGI AGSTNVTGDQ VKKLDVLSND LVINVLKSSF ATCVLVSEED 100
    KNAIIVEPEK RGKYVVCFDP LDGSSNIDCL VSIGTIFGIY RKNSTDEPSE 150
    KDALQPGRNL VAAGYALYGS ATMLVLAMVN GVNCFMLDPA IGEFILVDRD 200
    VKIKKKGSIY SINEGYAKEF DPAITEYIQR KKFPPDNSAP YGARYVGSMV 250
    ADVHRTLVYG GIFMYPANKK SPKGKLRLLY ECNPMAYVME KAGGLATTGK 300
    EAVLDIVPTD IHQRAPIILG SPEDVTELLE IYQKHAAK 338
    Length:338
    Mass (Da):36,779
    Last modified:January 23, 2007 - v4
    Checksum:i610BF8D3C6D320F6
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti2 – 21T → A AA sequence (PubMed:6291465)Curated
    Sequence conflicti4 – 41Q → E AA sequence (PubMed:6291465)Curated
    Sequence conflicti21 – 211E → Q AA sequence (PubMed:6296821)Curated
    Sequence conflicti97 – 971S → T AA sequence (PubMed:6296821)Curated
    Sequence conflicti157 – 1571G → E AA sequence (PubMed:6296821)Curated
    Sequence conflicti200 – 2001D → N AA sequence (PubMed:6296821)Curated
    Sequence conflicti229 – 2291Q → E AA sequence (PubMed:6296821)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M86347 mRNA. Translation: AAA31035.1.
    PIRiS37696. PAPGF.
    RefSeqiNP_999144.1. NM_213979.1.
    UniGeneiSsc.5127.

    Genome annotation databases

    GeneIDi397038.
    KEGGissc:397038.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M86347 mRNA. Translation: AAA31035.1 .
    PIRi S37696. PAPGF.
    RefSeqi NP_999144.1. NM_213979.1.
    UniGenei Ssc.5127.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1CNQ X-ray 2.27 A 2-338 [» ]
    1EYI X-ray 2.32 A 2-338 [» ]
    1EYJ X-ray 2.28 A/B 2-338 [» ]
    1EYK X-ray 2.23 A/B 2-338 [» ]
    1FBC X-ray 2.60 A/B 2-336 [» ]
    1FBD X-ray 2.90 A/B 2-336 [» ]
    1FBE X-ray 3.00 A/B 2-336 [» ]
    1FBF X-ray 2.70 A/B 2-336 [» ]
    1FBG X-ray 3.00 A/B 2-336 [» ]
    1FBH X-ray 2.50 A/B 2-336 [» ]
    1FBP X-ray 2.50 A/B 2-336 [» ]
    1FJ6 X-ray 2.50 A 2-338 [» ]
    1FJ9 X-ray 2.50 A/B 2-338 [» ]
    1FPB X-ray 2.60 A/B 2-336 [» ]
    1FPD X-ray 2.10 A/B 2-336 [» ]
    1FPE X-ray 2.20 A/B 2-336 [» ]
    1FPF X-ray 2.10 A/B 2-336 [» ]
    1FPG X-ray 2.30 A/B 2-336 [» ]
    1FPI X-ray 2.30 A/B 2-336 [» ]
    1FPJ X-ray 2.20 A/B 2-336 [» ]
    1FPK X-ray 3.00 A/B 2-336 [» ]
    1FPL X-ray 2.30 A/B 2-336 [» ]
    1FRP X-ray 2.00 A/B 2-336 [» ]
    1FSA X-ray 2.30 A/B 2-338 [» ]
    1KZ8 X-ray 2.00 A/F 2-338 [» ]
    1LEV X-ray 2.15 A/F 2-338 [» ]
    1NUW X-ray 1.30 A 2-338 [» ]
    1NUX X-ray 1.60 A 2-338 [» ]
    1NUY X-ray 1.30 A 2-338 [» ]
    1NUZ X-ray 1.90 A 2-338 [» ]
    1NV0 X-ray 1.80 A 2-338 [» ]
    1NV1 X-ray 1.90 A 2-338 [» ]
    1NV2 X-ray 2.10 A 2-338 [» ]
    1NV3 X-ray 2.00 A 2-338 [» ]
    1NV4 X-ray 1.90 A 2-338 [» ]
    1NV5 X-ray 1.90 A 2-338 [» ]
    1NV6 X-ray 2.15 A 2-338 [» ]
    1NV7 X-ray 2.15 A/B 2-338 [» ]
    1Q9D X-ray 2.35 A/B 2-338 [» ]
    1RDX X-ray 2.75 A/B 2-338 [» ]
    1RDY X-ray 2.20 A/B 2-338 [» ]
    1RDZ X-ray 2.05 A/B 2-338 [» ]
    1YXI X-ray 2.00 A 2-338 [» ]
    1YYZ X-ray 1.85 A 2-338 [» ]
    1YZ0 X-ray 2.07 A/B 2-338 [» ]
    2F3B X-ray 1.80 A 1-338 [» ]
    2F3D X-ray 1.83 A 1-338 [» ]
    2FBP X-ray 2.80 A/B 2-336 [» ]
    2QVU X-ray 1.50 A/B 2-338 [» ]
    2QVV X-ray 2.03 A/B 2-338 [» ]
    3FBP X-ray 2.80 A/B 2-336 [» ]
    4FBP X-ray 2.50 A/B/C/D 2-336 [» ]
    4GBV X-ray 2.90 A 2-336 [» ]
    4GBW X-ray 2.00 A 2-336 [» ]
    4GWS X-ray 2.75 A/B 2-338 [» ]
    4GWU X-ray 3.00 A 2-338 [» ]
    4GWW X-ray 3.20 A 2-338 [» ]
    4GWX X-ray 2.35 A 2-338 [» ]
    4GWY X-ray 3.00 A 2-338 [» ]
    4GWZ X-ray 2.60 A/B 2-338 [» ]
    4GX3 X-ray 2.25 A/B 2-338 [» ]
    4GX4 X-ray 2.50 A/B 2-338 [» ]
    4GX6 X-ray 2.50 A/B 2-338 [» ]
    4H45 X-ray 3.10 A 2-338 [» ]
    4H46 X-ray 2.50 A 2-338 [» ]
    4KXP X-ray 2.70 A/B 1-338 [» ]
    5FBP X-ray 2.10 A/B 2-336 [» ]
    ProteinModelPortali P00636.
    SMRi P00636. Positions 7-338.
    ModBasei Search...
    MobiDBi Search...

    Chemistry

    BindingDBi P00636.
    ChEMBLi CHEMBL2263.
    DrugBanki DB00131. Adenosine monophosphate.

    Proteomic databases

    PaxDbi P00636.
    PRIDEi P00636.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 397038.
    KEGGi ssc:397038.

    Organism-specific databases

    CTDi 2203.

    Phylogenomic databases

    eggNOGi COG0158.
    HOGENOMi HOG000191265.
    HOVERGENi HBG005627.
    KOi K03841.

    Enzyme and pathway databases

    UniPathwayi UPA00138 .
    BRENDAi 3.1.3.11. 6170.
    SABIO-RK P00636.

    Miscellaneous databases

    EvolutionaryTracei P00636.

    Family and domain databases

    HAMAPi MF_01855. FBPase_class1.
    InterProi IPR000146. FBPase_class-1/SBPase.
    IPR028343. FBPtase.
    IPR020548. Fructose_bisphosphatase_AS.
    [Graphical view ]
    PANTHERi PTHR11556. PTHR11556. 1 hit.
    Pfami PF00316. FBPase. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF500210. FBPtase. 1 hit.
    PIRSF000904. FBPtase_SBPase. 1 hit.
    PRINTSi PR00115. F16BPHPHTASE.
    PROSITEi PS00124. FBPASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Isolation and sequence analysis of the cDNA for pig kidney fructose 1,6-bisphosphatase."
      Williams M.K., Kantrowitz E.R.
      Proc. Natl. Acad. Sci. U.S.A. 89:3080-3082(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Kidney.
    2. "Complete amino acid sequence of pig kidney fructose-1,6-bisphosphatase."
      Marcus F., Edelstein I., Reardon I., Heinrikson R.L.
      Proc. Natl. Acad. Sci. U.S.A. 79:7161-7165(1982) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-336, ACETYLATION AT THR-2, PHOSPHORYLATION AT SER-208.
      Tissue: Kidney cortex.
    3. "Conservation of primary structure at the proteinase-sensitive site of fructose 1,6-bisphosphatases."
      McGregor J.S., Hannappel E., Xu G.-J., Pontremoli S., Horecker B.L.
      Arch. Biochem. Biophys. 217:652-664(1982) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-24 AND 44-61, ACETYLATION AT THR-2.
      Tissue: Kidney.
    4. "Mechanism of action of fructose 1,6-bisphosphatase."
      Benkovic S.J., Demaine M.M.
      Adv. Enzymol. Relat. Areas Mol. Biol. 53:45-82(1982) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBSTRATE-BINDING SITE, LIGANDS, REVIEW.
    5. "Structure refinement of fructose-1,6-bisphosphatase and its fructose 2,6-bisphosphate complex at 2.8-A resolution."
      Ke H.M., Thorpe C.M., Seaton B.A., Lipscomb W.N., Marcus F.
      J. Mol. Biol. 212:513-539(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH FRUCTOSE-2,6-BISPHOSPHATE, SEQUENCE REVISION.
    6. "Crystal structure of fructose-1,6-bisphosphatase complexed with fructose 6-phosphate, AMP, and magnesium."
      Ke H.M., Zhang Y.P., Lipscomb W.N.
      Proc. Natl. Acad. Sci. U.S.A. 87:5243-5247(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH FRUCTOSE-6-PHOSPHATE; AMP AND MAGNESIUM, ENZYME REGULATION, SUBUNIT.
    7. "Crystal structure of the neutral form of fructose-1,6-bisphosphatase complexed with the product fructose 6-phosphate at 2.1-A resolution."
      Ke H.M., Zhang Y.P., Liang J.-Y., Lipscomb W.N.
      Proc. Natl. Acad. Sci. U.S.A. 88:2989-2993(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH FRUCTOSE-6-PHOSPHATE.
    8. "Crystal structure of the neutral form of fructose 1,6-bisphosphatase complexed with regulatory inhibitor fructose 2,6-bisphosphate at 2.6-A resolution."
      Liang J.-Y., Huang S., Zhang Y.P., Ke H.M., Lipscomb W.N.
      Proc. Natl. Acad. Sci. U.S.A. 89:2404-2408(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH FRUCTOSE-2,6-BISPHOSPHATE.
    9. "Role of a dynamic loop in cation activation and allosteric regulation of recombinant porcine fructose-1,6-bisphosphatase."
      Choe J.-Y., Poland B.W., Fromm H.J., Honzatko R.B.
      Biochemistry 37:11441-11450(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.27 ANGSTROMS) IN COMPLEX WITH ZINC IONS, COFACTOR, ENZYME REGULATION.
    10. "Crystal structures of fructose 1,6-bisphosphatase: mechanism of catalysis and allosteric inhibition revealed in product complexes."
      Choe J.-Y., Fromm H.J., Honzatko R.B.
      Biochemistry 39:8565-8574(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.23 ANGSTROMS) IN COMPLEXES WITH FRUCTOSE-6-PHOSPHATE; PHOSPHATE; AMP; MAGNESIUM AND ZINC IONS, SUBUNIT, ENZYME REGULATION.
    11. "Metaphosphate in the active site of fructose-1,6-bisphosphatase."
      Choe J.-Y., Iancu C.V., Fromm H.J., Honzatko R.B.
      J. Biol. Chem. 278:16015-16020(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) IN COMPLEXES WITH MAGNESIUM IONS; FRUCTOSE-6-PHOSPHATE AND PHOSPHATE, COFACTOR, ENZYME MECHANISM.
    12. Cited for: X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) IN COMPLEX WITH THE SYNTHETIC INHIBITOR OC252; FRUCTOSE-6-PHOSPHATE; PHOSPHATE AND DIVALENT METAL CATIONS, COFACTOR, SUBUNIT, ENZYME REGULATION.
    13. "R-state AMP complex reveals initial steps of the quaternary transition of fructose-1,6-bisphosphatase."
      Iancu C.V., Mukund S., Fromm H.J., Honzatko R.B.
      J. Biol. Chem. 280:19737-19745(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF MUTANT LEU-55 IN COMPLEXES WITH AMP; FRUCTORSE-6-PHOSPHAT; PHOSPHATE AND MAGNESIUM IONS, SUBUNIT, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION.
    14. "Structures of mammalian and bacterial fructose-1,6-bisphosphatase reveal the basis for synergism in AMP/fructose 2,6-bisphosphate inhibition."
      Hines J.K., Chen X., Nix J.C., Fromm H.J., Honzatko R.B.
      J. Biol. Chem. 282:36121-36131(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) IN COMPLEXES WITH MAGNESIUM IONS AND FRUCTOSE-2,6-DIPHOSPHATE, SUBUNIT, ENZYME REGULATION.

    Entry informationi

    Entry nameiF16P1_PIG
    AccessioniPrimary (citable) accession number: P00636
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 134 of the entry and version 4 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    The molecule has a highly reactive cysteine residue (Cys-117 or Cys-129), which tends to form mixed disulfides (e.g. with homocystine) but is not essential for enzyme activity.

    Keywords - Technical termi

    3D-structure, Allosteric enzyme, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3